ID A0A2V3JK82_9EURY Unreviewed; 1830 AA.
AC A0A2V3JK82;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 02-APR-2025, entry version 25.
DE RecName: Full=PKD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=C4B59_10120 {ECO:0000313|EMBL:PXF60060.1};
OS ANME-2 cluster archaeon.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Methanomicrobia; Methanosarcinales; ANME-2 cluster.
OX NCBI_TaxID=2056317 {ECO:0000313|EMBL:PXF60060.1, ECO:0000313|Proteomes:UP000248329};
RN [1] {ECO:0000313|EMBL:PXF60060.1, ECO:0000313|Proteomes:UP000248329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E20ANME2 {ECO:0000313|EMBL:PXF60060.1};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PXF60060.1}.
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DR EMBL; PQXF01000019; PXF60060.1; -; Genomic_DNA.
DR Proteomes; UP000248329; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd14256; Dockerin_I; 1.
DR CDD; cd07473; Peptidases_S8_Subtilisin_like; 1.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 1.10.1330.10; Dockerin domain; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR002105; Dockerin_1_rpt.
DR InterPro; IPR036439; Dockerin_dom_sf.
DR InterPro; IPR054399; Fervidolysin-like_N_prodom.
DR InterPro; IPR022790; GH26_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR007742; NosD_dom.
DR InterPro; IPR022441; Para_beta_helix_rpt-2.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR051048; Peptidase_S8/S53_subtilisin.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034204; PfSUB1-like_cat_dom.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR NCBIfam; TIGR03804; para_beta_helix; 2.
DR PANTHER; PTHR43399:SF4; CELL WALL-ASSOCIATED PROTEASE; 1.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF07705; CARDB; 2.
DR Pfam; PF00404; Dockerin_1; 1.
DR Pfam; PF22148; Fervidolysin_NPro-like; 1.
DR Pfam; PF05048; NosD; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF18911; PKD_4; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SMART; SM00722; CASH; 2.
DR SMART; SM00710; PbH1; 14.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR SUPFAM; SSF63446; Type I dockerin domain; 1.
DR PROSITE; PS51764; GH26; 1.
DR PROSITE; PS50093; PKD; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 1255..1338
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1327..1664
FT /note="GH26"
FT /evidence="ECO:0000259|PROSITE:PS51764"
FT ACT_SITE 913
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 968
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1128
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR615500-1,
FT ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1830 AA; 198984 MW; 687099549BE5BA7B CRC64;
MKHIIATLII LASLTPAAGA TQLYVNEIGW WIDPAQFNAS STPIQSAIDN AIGGDSIHVY
NGSYTDNIRI DKDLTVEGED RDTTVIDGGG SGDCVRVSSA DVIISGFTIK NAGGYGIYAY
KSALNLDNAT ITDCGNDAIY FKDGKSLTLR DSVLENCGDG LYYHNSAAGN ATIEGNVIRD
TTGYGLKVWL ASGNSAVIAD NLIINSTGTY SDGIYCYISG TGKSLTVANN TVKNSGDDGV
YLVGAINVTI TNTTVDTAGD YGIYAPGCDL SINKATIRNC GNDAIYFKDG KSLTLRDSVL
ENCGDGLYYH NSAAGNATIE RNIIRNNTGS GLFIKLASEK STVINDNMIL NNTGSDSDGI
YCYISGDGGL VTLQNNTVKN SGDDGIHLSG AKYSTLFNNT ISLNSAYGIG LYSSNSNLIF
HNNLVNNSPN AYDSNPTSND WHHPILLEGN YWSDYTGIDD GSGTGKHAIA GDGIGDTNIP
HPGPNYDSYP FVNESRWTWP KLKIVQAHTD KITYVLDETA TIYCVVQSET GVNISVDNIT
AKIIKPDSST EWITLIEGSI GNYKAIFTNT SLFGTYDVTI YANKIGYVTD AAKLGFEVLA
EHDIAVTNID APGSTEVDST IIVDAPIGNI GLNNESNITV GFIVDGVNQS NITIPFLKSR
SYTNVSFQWT APSVAGMHNI TIYAEPVVNE TIVWNNRLNK IISVITIADI WVNPKSFDIN
LSHGSITNKT LTIGNNGTGT SVFNITSMGA ETSLDSFEIR KYNIDTLENI DILKSKIHRN
KFDTSLLKYE HKPGELLVKY IKNFSTLDTE DFYMSQNATL IKDYPESGYH LIRVDESKLE
ETIEILAKSG LFEAAEPNYI LKAIGIPNDP RFNELWGMHN IGQTGGTADA DIDAAEAWGI
FTGNKKVIVA VIDTGVDYNH EDLANNMWTN PGEIPSNGID DDGNGFVDDY YGWDFAYNDN
DPMDGHSHGT HCSGTIGGVG NNGVGVAGVS WDVRIMAVKY LSDVGRGSTS DAIDAINYAS
MMGADIMSNS WGGGPHSSAL EAAIQAADNA GILFVAAAGN DKKNTDIYPH YPSCYGVPNV
MSIAATNHND ARAGFSNYGN LTVDLGAPGV SILSSVPGNG YSSHSGTSMA TPHVAGAAAL
LKALNPALTH LEIKNILMNS VDPLTSLYGK TVTGGRLNMH KAITSISPPW LSVSPTNGSI
PAGRQINVIV RINATNLNEN IYNSTIVIKN NDPDENPVTI PVNLTVTVSE PNQPPIANFT
YSPPNPVENQ TITFNASSSY DPDGNITNYK WHFGDGNITN TIEEIIRHSY SLESNYNVCL
TVTDNDGATN SISKTIRISN LTGCYIGAYL GCGSEDLSCE SISEFNHKMG KNHTIFVRYV
DIKDSRNPSH WDWAEEVKRN SAMPMFIYDP YDGLDNINTG DVEYFASKCK EFNETVLIVF
GHEMNGPWHS WGNDPENYTN KFKEVAEIFH REAPKVEMCW APNQNWGYPW GGVDYGDGYS
EYYPEGIGAY GEYVDWVGLN FYEKDWDEDD LIPPDMFIAN IRWGDDGTDF YKMFAEEKNK
PMLIAETGAF DPNKDTTPPG ERNPLNEMEQ ATFKNEWLNQ VYNVSTLKGE FPRLNAICYF
HVEKRELIDT QTHSFYDIVV DYRIPESPNV YKNLISDSYF LSSAITPVTN PDLVILEKWV
CWLCNCTIYY NVTNIGNGTA PACHNTTLYV DGDEEAHDHV PVDLAPGESY TGCFDNYNRT
YTPPSENITV CADSGDVVTE LNETNNCLAC VWKCGDLNND NQITPADAAI ALQLAASGAQ
NPAADMNDDG CITSLDALMI LQAAAGRIEL
//
